The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.
Identifieur interne : 001298 ( Ncbi/Merge ); précédent : 001297; suivant : 001299The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.
Auteurs : Hui Fan ; Amy Ooi ; Yong Wah Tan ; Sifang Wang ; Shouguo Fang ; Ding Xiang Liu ; Julien LescarSource :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Nucleocapsid.
- chemical , metabolism : Nucleocapsid Proteins, RNA.
- Amino Acid Sequence, Crystallography, Dimerization, Infectious bronchitis virus, Molecular Sequence Data, Protein Structure, Tertiary.
Abstract
The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.
DOI: 10.1016/j.str.2005.08.021
PubMed: 16338414
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sortKey="Fang, Shouguo" sort="Fang, Shouguo" uniqKey="Fang S" first="Shouguo" last="Fang">Shouguo Fang</name></author><author><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name></author><author><name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</name></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography</term><term>Dimerization</term><term>Infectious bronchitis virus</term><term>Molecular Sequence Data</term><term>Nucleocapsid (chemistry)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Structure, Tertiary</term><term>RNA (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN (métabolisme)</term><term>Cristallographie</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Nucléocapside ()</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus de la bronchite infectieuse</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>RNA</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography</term><term>Dimerization</term><term>Infectious bronchitis virus</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallographie</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Nucléocapside</term><term>Protéines nucléocapside</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus de la bronchite infectieuse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16338414</PMID><DateCompleted><Year>2006</Year><Month>02</Month><Day>03</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0969-2126</ISSN><JournalIssue CitedMedium="Print"><Volume>13</Volume><Issue>12</Issue><PubDate><Year>2005</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Structure (London, England : 1993)</Title><ISOAbbreviation>Structure</ISOAbbreviation></Journal><ArticleTitle>The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties.</ArticleTitle><Pagination><MedlinePgn>1859-68</MedlinePgn></Pagination><Abstract><AbstractText>The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fan</LastName><ForeName>Hui</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ooi</LastName><ForeName>Amy</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Yong Wah</ForeName><Initials>YW</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Sifang</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Shouguo</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Ding Xiang</ForeName><Initials>DX</Initials></Author><Author ValidYN="Y"><LastName>Lescar</LastName><ForeName>Julien</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Structure</MedlineTA><NlmUniqueID>101087697</NlmUniqueID><ISSNLinking>0969-2126</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003461" MajorTopicYN="N">Crystallography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001351" MajorTopicYN="Y">Infectious bronchitis virus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019251" MajorTopicYN="N">Nucleocapsid</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" 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Oct;11(10):1219-26</Citation><ArticleIdList><ArticleId IdType="pubmed">14527390</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 May 14;317(4):1030-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15094372</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 1992 Jun;66(6):3522-30</Citation><ArticleIdList><ArticleId IdType="pubmed">1316465</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2001 Feb;75(3):1312-24</Citation><ArticleIdList><ArticleId IdType="pubmed">11152504</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1986 Apr 30;150(2):402-10</Citation><ArticleIdList><ArticleId IdType="pubmed">3083580</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2004 Feb;12(2):341-53</Citation><ArticleIdList><ArticleId IdType="pubmed">14962394</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2025413</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2002 May;76(10):4987-99</Citation><ArticleIdList><ArticleId IdType="pubmed">11967315</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 1997 Aug 1;270(5):724-38</Citation><ArticleIdList><ArticleId IdType="pubmed">9245600</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1996 Mar 1;217(1):191-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8599203</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 May 25;43(20):6059-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15147189</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2003 Mar;77(5):2922-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12584316</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation><ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2003 Jul;77(14):7890-902</Citation><ArticleIdList><ArticleId IdType="pubmed">12829829</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation><ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7149-54</Citation><ArticleIdList><ArticleId IdType="pubmed">10377383</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virus Res. 2000 Mar;67(1):31-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10773316</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods Enzymol. 1997;276:523-30</Citation><ArticleIdList><ArticleId IdType="pubmed">9048379</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Apr 2;316(2):476-83</Citation><ArticleIdList><ArticleId IdType="pubmed">15020242</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Lancet. 2003 May 24;361(9371):1767-72</Citation><ArticleIdList><ArticleId IdType="pubmed">12781535</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21</Citation><ArticleIdList><ArticleId IdType="pubmed">9757107</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2000 Sep;74(17):8127-34</Citation><ArticleIdList><ArticleId IdType="pubmed">10933723</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>EMBO J. 1996 Apr 15;15(8):2020-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8617249</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 1998 Jan 16;279(5349):384-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9430589</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2003 Nov;11(11):1445-51</Citation><ArticleIdList><ArticleId IdType="pubmed">14604534</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virus Res. 1992 Sep 15;25(3):213-22</Citation><ArticleIdList><ArticleId IdType="pubmed">1332275</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods Enzymol. 2003;374:22-37</Citation><ArticleIdList><ArticleId IdType="pubmed">14696367</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2000 Jan;74(1):580-3</Citation><ArticleIdList><ArticleId IdType="pubmed">10590153</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2005 Apr 25;579(11):2387-96</Citation><ArticleIdList><ArticleId IdType="pubmed">15848177</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1967-70</Citation><ArticleIdList><ArticleId IdType="pubmed">10666571</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 1980 Jan;33(1):449-62</Citation><ArticleIdList><ArticleId IdType="pubmed">6245243</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell. 2001 Apr 6;105(1):137-48</Citation><ArticleIdList><ArticleId IdType="pubmed">11301009</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>PLoS Biol. 2005 Jan;3(1):e5</Citation><ArticleIdList><ArticleId IdType="pubmed">15630477</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 1993 Sep 5;233(1):123-38</Citation><ArticleIdList><ArticleId IdType="pubmed">8377180</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2004 Jul;12(7):1157-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15242592</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Anal Chem. 2005 Jun 1;77(11):3466-78</Citation><ArticleIdList><ArticleId IdType="pubmed">15924377</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Fan, Hui" sort="Fan, Hui" uniqKey="Fan H" first="Hui" last="Fan">Hui Fan</name><name sortKey="Fang, Shouguo" sort="Fang, Shouguo" uniqKey="Fang S" first="Shouguo" last="Fang">Shouguo Fang</name><name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</name><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name><name sortKey="Ooi, Amy" sort="Ooi, Amy" uniqKey="Ooi A" first="Amy" last="Ooi">Amy Ooi</name><name sortKey="Tan, Yong Wah" sort="Tan, Yong Wah" uniqKey="Tan Y" first="Yong Wah" last="Tan">Yong Wah Tan</name><name sortKey="Wang, Sifang" sort="Wang, Sifang" uniqKey="Wang S" first="Sifang" last="Wang">Sifang Wang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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